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Biochem Biophys Res Commun. 2013 Oct 18;440(2):271-6. doi: 10.1016/j.bbrc.2013.09.064. Epub 2013 Sep 19.

Asymmetric packaging of polymerases within vesicular stomatitis virus.

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  • 1Dept. of Physics and Astronomy, University of Utah, United States; Center for Cell and Genome Science, University of Utah, United States.


Vesicular stomatitis virus (VSV) is a prototypic negative sense single-stranded RNA virus. The bullet-shape appearance of the virion results from tightly wound helical turns of the nucleoprotein encapsidated RNA template (N-RNA) around a central cavity. Transcription and replication require polymerase complexes, which include a catalytic subunit L and a template-binding subunit P. L and P are inferred to be in the cavity, however lacking direct observation, their exact position has remained unclear. Using super-resolution fluorescence imaging and atomic force microscopy (AFM) on single VSV virions, we show that L and P are packaged asymmetrically towards the blunt end of the virus. The number of L and P proteins varies between individual virions and they occupy 57 ± 12 nm of the 150 nm central cavity of the virus. Our finding positions the polymerases at the opposite end of the genome with respect to the only transcriptional promoter.

Copyright © 2013 The Authors. Published by Elsevier Inc. All rights reserved.


AFM; L protein; P protein; PALM; Polymerase; RdRP; STORM; VSV; Viral replication

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